Enzyme hyperspecificity. Rejection of threonine by the valyl-tRNA synthetase by misacylation and hydrolytic editing
about
Structure of crystalline D-Tyr-tRNA(Tyr) deacylase. A representative of a new class of tRNA-dependent hydrolasesCrystal structures of the CP1 domain from Thermus thermophilus isoleucyl-tRNA synthetase and its complex with L-valineMechanistic insights into cognate substrate discrimination during proofreading in translationPeripheral insertion modulates the editing activity of the isolated CP1 domain of leucyl-tRNA synthetaseYeast mitochondrial threonyl-tRNA synthetase recognizes tRNA isoacceptors by distinct mechanisms and promotes CUN codon reassignmentThe physiological target for LeuRS translational quality control is norvalinePartition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifsValyl-tRNA synthetase from Escherichia coli MALDI-MS identification of the binding sites for L-valine or for noncognate amino acids upon qualitative comparative labeling with reactive amino-acid analogs.Discovery of aminoacyl-tRNA synthetase activity through cell-surface display of noncanonical amino acidsProofreading in vivo: editing of homocysteine by methionyl-tRNA synthetase in Escherichia coliSevere oxidative stress induces protein mistranslation through impairment of an aminoacyl-tRNA synthetase editing site.The balance between pre- and post-transfer editing in tRNA synthetases.A paradigm shift for the amino acid editing mechanism of human cytoplasmic leucyl-tRNA synthetase.Transfer RNA determinants for translational editing by Escherichia coli valyl-tRNA synthetasePartitioning of tRNA-dependent editing between pre- and post-transfer pathways in class I aminoacyl-tRNA synthetases.Proofreading in translation: dynamics of the double-sieve modelRelaxed substrate specificity leads to extensive tRNA mischarging by Streptococcus pneumoniae class I and class II aminoacyl-tRNA synthetasesTryptophanyl-tRNA synthetase Urzyme: a model to recapitulate molecular evolution and investigate intramolecular complementationFunctional group recognition at the aminoacylation and editing sites of E. coli valyl-tRNA synthetase.Interstice mutations that block site-to-site translocation of a misactivated amino acid bound to a class I tRNA synthetase.Modular pathways for editing non-cognate amino acids by human cytoplasmic leucyl-tRNA synthetaseMolecular mechanism of co-translational protein targeting by the signal recognition particleExperimental evidence for kinetic proofreading in the aminoacylation of tRNA by synthetaseEditing of errors in selection of amino acids for protein synthesisKinetic partitioning between synthetic and editing pathways in class I aminoacyl-tRNA synthetases occurs at both pre-transfer and post-transfer hydrolytic stepsCrystallization and preliminary X-ray crystallographic study of alanyl-tRNA synthetase from the archaeon Archaeoglobus fulgidusCrucial role of the C-terminal domain of Mycobacterium tuberculosis leucyl-tRNA synthetase in aminoacylation and editing.Misactivated amino acids translocate at similar rates across surface of a tRNA synthetase.p53-Dependent DNA damage response sensitive to editing-defective tRNA synthetase in zebrafish.Primary Structure Revision and Active Site Mapping of E. Coli Isoleucyl-tRNA Synthetase by Means of Maldi Mass SpectrometryDNA polymerases and aminoacyl-tRNA synthetases: shared mechanisms for ensuring the fidelity of gene expressionA domain for editing by an archaebacterial tRNA synthetaseSignal recognition particle: an essential protein-targeting machine.Co-translational protein targeting to the bacterial membrane.Fidelity of cotranslational protein targeting by the signal recognition particle.Rewiring protein synthesis: From natural to synthetic amino acids.Threonyl-tRNA synthetase from yeast: aminoacylation of tRNA on its non-accepting 3'-terminal hydroxyl group and its behaviour in enzyme-catalyzed deacylation.Amino acid:tRNA ligases (EC 6.1.1..-).The proofreading of hydroxy analogues of leucine and isoleucine by leucyl-tRNA synthetases from E. coli and yeast.Induced hydrolytic activity of yeast phenylalanyl-tRNA synthetase by tRNAPhe-CC.
P2860
Q27634982-5E6FBC49-3F85-473D-9FEF-8A9F359FCA68Q27642781-24F7595E-8463-4FCD-AF57-9EA641933A30Q27666037-49E8AE4F-54A5-404B-9D62-E1980CC5D261Q27671550-27B08335-494A-4A90-9424-21CD7D966C85Q27677330-D7EF7886-F988-472B-A392-56BD3E0C8950Q27684356-AF73E58A-6011-46B0-AEDB-F3F3F6A84F71Q29616422-3C2D5551-D3E2-49F3-812E-B2B4EC65F4B3Q30886705-57F64B1D-4D12-4E01-AC85-08C7B18BE627Q33248009-68B94195-9AA2-4800-A1BE-45ACEA9BEB3CQ33630717-0DDC680C-227B-4E23-8973-338502869B72Q33733028-C8BF3794-1A72-4C40-95B1-BF2BEF3808E8Q33810666-AA0774D0-4E1D-4309-BCA4-D9E76C96B754Q33856267-742DEA3A-A853-4CB0-8895-7702C814E343Q33891427-899B9C19-B83C-4944-905A-8476116ECC31Q34025372-ABA115A1-1E96-4887-A8A6-9E1ECEBA78BEQ34154464-DC53A103-FD42-4DD7-BFA4-A07213AB824DQ34237902-19FFEB91-1930-407C-A6E9-FC93F55A983EQ34352343-9B1CC33D-5641-4ACD-92C9-776E36054DE0Q34366948-43546AF5-BF06-4241-A073-2AED274E820BQ34469989-17217026-B89C-4C33-98A5-D1607E270725Q34474121-0A06A304-DA34-4C7D-9379-4BA0223E5A84Q34797147-D04046D1-911B-495B-82EA-A04A668A1B75Q35063202-A6FD89FF-D187-4A03-9B8C-5FE86B240C8EQ35403101-60DC9E51-B6EA-420D-AD0A-01E91C965018Q36127172-2E271618-C19D-4E7E-BD86-59BC75BECFBFQ36580552-13ED4EC4-3E36-40B8-8F57-768D5D73A9E8Q36580862-4B49493A-03CB-4001-8451-49D497F18273Q36963357-9C068B5B-35CF-4293-9D4B-F85C655CC530Q37142865-727B8B2D-69DE-4777-ACE4-AA8E235ADA12Q37225462-3BB66705-A10E-4BAB-A373-576D6817C973Q37292570-0A9E53EE-BA78-449D-8010-BC2B4120F2FEQ37646125-A2B92F55-D445-46A9-8BFB-4618F2CB8DB8Q38081948-E33FFCD8-2E4C-4A96-B35F-11988A2D41B4Q38186912-B3423D00-89C9-421F-9AA1-C2384ECFD3CFQ38217500-969A0760-D7C0-40E2-BCAC-0652F9AF5F53Q39092037-61493952-917F-4CF4-B95D-CEAA4F198935Q40151707-4B6FB97D-0DC7-46F4-A548-167ECDA9E7E3Q40293016-5332810C-F386-4698-9F7C-2F1164FEFD87Q40418842-DC424ED0-5333-4059-B1D8-96D5FF9191E3Q40464189-28B8003E-7B6F-428B-A791-682BCD5C3D2D
P2860
Enzyme hyperspecificity. Rejection of threonine by the valyl-tRNA synthetase by misacylation and hydrolytic editing
description
1976 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1976 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1976
@ast
im Juli 1976 veröffentlicher wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1976/07/27)
@sk
vědecký článek publikovaný v roce 1976
@cs
wetenschappelijk artikel (gepubliceerd op 1976/07/27)
@nl
наукова стаття, опублікована в липні 1976
@uk
مقالة علمية (نشرت في 27-7-1976)
@ar
name
Enzyme hyperspecificity. Rejec ...... ylation and hydrolytic editing
@ast
Enzyme hyperspecificity. Rejec ...... ylation and hydrolytic editing
@en
Enzyme hyperspecificity. Rejec ...... ylation and hydrolytic editing
@nl
type
label
Enzyme hyperspecificity. Rejec ...... ylation and hydrolytic editing
@ast
Enzyme hyperspecificity. Rejec ...... ylation and hydrolytic editing
@en
Enzyme hyperspecificity. Rejec ...... ylation and hydrolytic editing
@nl
prefLabel
Enzyme hyperspecificity. Rejec ...... ylation and hydrolytic editing
@ast
Enzyme hyperspecificity. Rejec ...... ylation and hydrolytic editing
@en
Enzyme hyperspecificity. Rejec ...... ylation and hydrolytic editing
@nl
P356
P1433
P1476
Enzyme hyperspecificity. Rejec ...... ylation and hydrolytic editing
@en
P2093
A. R. Fersht
M. M. Kaethner
P304
P356
10.1021/BI00660A026
P407
P577
1976-07-27T00:00:00Z